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J Biol Chem. 2015 Jul 31;290(31):18991-8. doi: 10.1074/jbc.R115.645085. Epub 2015 Jun 8.

Nutritional Immunity: S100 Proteins at the Host-Pathogen Interface.

Author information

1
From the Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232 and.
2
the Departments of Biochemistry and Chemistry, and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232.
3
From the Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232 and Eric.skaar@Vanderbilt.edu.

Abstract

The S100 family of EF-hand calcium (Ca(2+))-binding proteins is essential for a wide range of cellular functions. During infection, certain S100 proteins act as damage-associated molecular patterns (DAMPs) and interact with pattern recognition receptors to modulate inflammatory responses. In addition, these inflammatory S100 proteins have potent antimicrobial properties and are essential components of the immune response to invading pathogens. In this review, we focus on S100 proteins that exhibit antimicrobial properties through the process of metal limitation, termed nutritional immunity, and discuss several recent advances in our understanding of S100 protein-mediated metal sequestration at the site of infection.

KEYWORDS:

S100 proteins; S100A12; S100A7; bacteria; calprotectin; host-pathogen interaction; immunology; microbiology; nutritional immunity

PMID:
26055713
PMCID:
PMC4521021
DOI:
10.1074/jbc.R115.645085
[Indexed for MEDLINE]
Free PMC Article

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